Erratum to: The p66Shc redox adaptor protein is induced by saturated fatty acids and mediates lipotoxicity-induced apoptosis in pancreatic beta cells [Diabetologia, DOI 10.1007/s00125-015-3563-2];The p66Shc redox adaptor protein is induced by saturated fatty acids and mediates lipotoxicity-induced apoptosis in pancreatic beta cells

Diabetologia

Volumn 58, Issue 6, 2015, Pages 1260-1271

  Natalicchio, Annalisa ^a,b,c,d,e   Tortosa, Federica ^a,b,c,d,e   Labarbuta, Rossella ^a,b,c,d,e   Biondi, Giuseppina ^a,b,c,d,e   Marrano, Nicola ^a,b,c,d,e   Carchia, Emanuele ^a,b,c,d,e   Leonardini, Anna ^a,b,c,d,e   Cignarelli, Angelo ^a,b,c,d,e   Bugliani, Marco ^a,b,c,d,e   Marchetti, Piero ^a,b,c,d,e   Fadini, Gian Paolo ^a,b,c,d,e   Giorgio, Marco ^a,b,c,d,e   Avogaro, Angelo ^a,b,c,d,e   Perrini, Sebastio ^a,b,c,d,e   Laviola, Luigi ^a,b,c,d,e   Giorgino, Francesco ^a,b,c,d,e  

^a UNIVERSITY OF BARI   (Italy)

^b Grande Ospedale Metropolitano   (Italy)

^c UNIVERSITY OF PISA   (Italy)

^d VENETIAN INSTITUTE OF MOLECULAR MEDICINE   (Italy)

^e EUROPEAN INSTITUTE OF ONCOLOGY   (Italy)

Author keywords

Apoptosis; Beta cell; Exendin 4; JNK; p53; p66Shc; Palmitic acid; Pancreatic islet

Indexed keywords

FATTY ACID; PROTEIN P53; PROTEIN SHC; REACTIVE OXYGEN METABOLITE; SHC1 PROTEIN, HUMAN; SHC1 PROTEIN, MOUSE; SHC1 PROTEIN, RAT; SMALL INTERFERING RNA; TP53 PROTEIN, HUMAN;

ADENOVIRIDAE; AGED; ANIMAL; APOPTOSIS; BODY MASS; C57BL MOUSE; CYTOLOGY; FEMALE; GENE EXPRESSION PROFILING; GENETICS; HUMAN; LIPID DIET; MALE; METABOLISM; MIDDLE AGED; MOUSE; OXIDATION REDUCTION REACTION; PANCREAS ISLET BETA CELL; PHOSPHORYLATION; RAT; SIGNAL TRANSDUCTION; TRANSGENIC MOUSE;

ADENOVIRIDAE; AGED; ANIMALS; APOPTOSIS; BODY MASS INDEX; DIET, HIGH-FAT; FATTY ACIDS; FEMALE; GENE EXPRESSION PROFILING; HUMANS; INSULIN-SECRETING CELLS; MALE; MICE; MICE, INBRED C57BL; MICE, TRANSGENIC; MIDDLE AGED; OXIDATION-REDUCTION; PHOSPHORYLATION; RATS; REACTIVE OXYGEN SPECIES; RNA, SMALL INTERFERING; SHC SIGNALING ADAPTOR PROTEINS; SIGNAL TRANSDUCTION; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84939942881     PISSN: 0012186X     EISSN: 14320428     Source Type: Journal    
DOI: 10.1007/s00125-015-3739-9     Document Type: Erratum

References (50)

1. Paolisso G, Tataranni PA (1995) A high concentration of fasting plasma non-esterified fatty acids is a risk factor for the development of NIDDM. Diabetologia 38:1213–1217
2. Shimabukuro M, Zhou YT, Levi M, Unger RH (1998) Fatty acid-induced beta cell apoptosis: a link between obesity and diabetes. Proc Natl Acad Sci U S A 95:2498–2502
3. McGarry JD, Dobbins RL (1999) Fatty acids, lipotoxicity and insulin secretion. Diabetologia 42:128–138
4. Cunha DA, Hekerman P, Ladrière L et al (2008) Initiation and execution of lipotoxic ER stress in pancreatic beta cells. J Cell Sci 121(Pt 14):2308–2318
5. Lameloise N, Muzzin P, Prentki M, Assimacopoulos-Jeannet F (2001) Uncoupling protein 2: a possible link between fatty acid excess and impaired glucose-induced insulin secretion? Diabetes 50:803–809
6. Natalicchio A, Labarbuta R, Tortosa F et al (2013) Exendin-4 protects pancreatic beta cells from palmitate-induced apoptosis by interfering with GPR40 and the MKK4/7 stress kinase signalling pathway. Diabetologia 56:2456–2466
7. Yuan H, Zhang X, Huang X et al (2010) NADPH oxidase 2-derived reactive oxygen species mediate FFAs-induced dysfunction and apoptosis of β-cells via JNK, p38 MAPK and p53 pathways. PLoS One 5:e15726
8. Eitel K, Staiger H, Rieger J et al (2003) Protein kinase C delta activation and translocation to the nucleus are required for fatty acid-induced apoptosis of insulin-secreting cells. Diabetes 52:991–997
9. Gehrmann W, Elsner M, Lenzen S (2010) Role of metabolically generated reactive oxygen species for lipotoxicity in pancreatic β-cells. Diabetes Obes Metab 12(Suppl 2):149–158
10. Wrede CE, Dickson LM, Lingohr MK, Briaud I, Rhodes CJ (2002) Protein kinase B/Akt prevents fatty acid-induced apoptosis in pancreatic beta cells (INS-1). J Biol Chem 277:49676–49684
11. Luzi L, Confalonieri S, Di Fiore PP, Pelicci PG (2000) Evolution of Shc functions from nematode to human. Curr Opin Genet Dev 10:668–674
12. Natalicchio A, Tortosa F, Perrini S, Laviola L, Giorgino F (2011) p66Shc, a multifaceted protein linking Erk signalling, glucose metabolism, and oxidative stress. Arch Physiol Biochem 117:116–124
13. Migliaccio E, Mele S, Salcini AE et al (1997) Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway. EMBO J 16:706–716
14. Okada S, Kao AW, Ceresa BP, Blaikie P, Margolis B, Pessin JE (1997) The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen-activated protein kinase pathway. J Biol Chem 272:28042–28049
15. Arany I, Faisal A, Nagamine Y, Safirstein RL (2008) p66shc inhibits pro-survival epidermal growth factor receptor/ ERK signaling during severe oxidative stress in mouse renal proximal tubule cells. J Biol Chem 283:6110–6117
16. Natalicchio A, Laviola L, de Tullio C (2004) Role of the p66Shc isoform in insulin-like growth factor I receptor signaling through MEK/Erk and regulation of actin cytoskeleton in rat myoblasts. J Biol Chem 279:43900–43909
17. Natalicchio A, de Stefano F, Perrini S et al (2009) Involvement of the p66Shc protein in glucose transport regulation in skeletal muscle myoblasts. Am J Physiol Endocrinol Metab 296:E228–E237
18. Migliaccio E, Giorgio M, Mele S et al (1999) The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 402:309–313
19. Menini S, Amadio L, Oddi G et al (2006) Deletion of p66Shc longevity gene protects against experimental diabetic glomerulopathy by preventing diabetes-induced oxidative stress. Diabetes 55:1642–1650
20. Albiero M, Poncina N, Tjwa M et al (2014) Diabetes causes bone marrow autonomic neuropathy and impairs stem cell mobilization via dysregulated p66Shc and Sirt1. Diabetes 63:1353–1365
21. Pagnin E, Fadini G, de Toni R, Tiengo A, Calò L, Avogaro A (2005) Diabetes induces p66shc gene expression in human peripheral blood mononuclear cells: relationship to oxidative stress. J Clin Endocrinol Metab 90:1130–1136
22. Trinei M, Giorgio M, Cicalese A et al (2002) A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis. Oncogene 21:3872–3878
23. Kim CS, Jung SB, Naqvi A et al (2008) P53 impairs endothelium-dependent vasomotor function through transcriptional upregulation of p66Shc. Circ Res 103:1441–1450
24. de Kreutzenberg SV, Ceolotto G, Papparella I et al (2010) Downregulation of the longevity-associated protein sirtuin 1 in insulin resistance and metabolic syndrome: potential biochemical mechanisms. Diabetes 59:1006–1015
25. Li DS, Yuan YH, Tu HJ, Liang QL, Dai LJ (2009) A protocol for islet isolation from mouse pancreas. Nat Protoc 4:1649–1652
26. Lupi R, del Guerra S, Fierabracci V et al (2002) Lipotoxicity in human pancreatic islets and the protective effect of metformin. Diabetes 51(Suppl 1):S134–S137
27. Santangelo C, Scipioni A, Marselli L, Marchetti P, Dotta F (2005) Suppressor of cytokine signaling gene expression in human pancreatic islets: modulation by cytokines. Eur J Endocrinol 152:485–489
28. Natalicchio A, de Stefano F, Orlando MR et al (2010) Exendin-4 prevents c-Jun N-terminal protein kinase activation by tumor necrosis factor-alpha (TNFalpha) and inhibits TNFalpha-induced apoptosis in insulin-secreting cells. Endocrinology 151:2019–2029
29. Prentki M, Nolan CJ (2006) Islet beta cell failure in type 2 diabetes. J Clin Invest 116:1802–1812
30. Wilding JP (2007) The importance of free fatty acids in the development of type 2 diabetes. Diabet Med 24:934–945
31. Azevedo-Martins AK, Monteiro AP, Lima CL, Lenzen S, Curi R (2006) Fatty acid-induced toxicity and neutral lipid accumulation in insulin-producing RINm5F cells. Toxicol In Vitro 20:1106–1113
32. Karaskov E, Scott C, Zhang L, Teodoro T, Ravazzola M, Volchuk A (2006) Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta cell apoptosis. Endocrinology 147:3398–3407
33. Wang HJ, Lee EY, Han SJ et al (2012) Dual pathways of p53 mediated glucolipotoxicity-induced apoptosis of rat cardiomyoblast cell: activation of p53 proapoptosis and inhibition of Nrf2-NQO1 antiapoptosis. Metabolism 61:496–503
34. Tomita K, Teratani T, Suzuki T et al (2012) p53/p66Shc-mediated signaling contributes to the progression of non-alcoholic steatohepatitis in humans and mice. J Hepatol 57:837–843
35. Yang CP, Horwitz SB (2000) Taxol mediates serine phosphorylation of the 66-kDa Shc isoform. Cancer Res 60:5171–5178
36. Smith WW, Norton DD, Gorospe M (2005) Phosphorylation of p66Shc and forkhead proteins mediates Abeta toxicity. J Cell Biol 169:331–339
37. Napoli C, Martin-Padura I, de Nigris F et al (2003) Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet. Proc Natl Acad Sci U S A 100:2112–2116
38. Hu Y, Wang X, Zeng L et al (2005) ERK phosphorylates p66ShcA on Ser36 and subsequently regulates p27kip1 expression via the Akt-FoxO3a pathway: implication of p27kip1 in cell response to oxidative stress. Mol Biol Cell 16:3705–3718
39. Le S, Connors TJ, Maroney AC (2001) c-Jun N-terminal kinase specifically phosphorylates p66ShcA at serine 36 in response to ultraviolet irradiation. J Biol Chem 276:48332–48336
40. Foschi M, Franchi F, Han J, La Villa G, Sorokin A (2001) Endothelin-1 induces serine phosphorylation of the adaptor protein p66Shc and its association with 14-3-3 protein in glomerular mesangial cells. J Biol Chem 276:26640–26647
41. Yang CP, Horwitz SB (2002) Distinct mechanisms of taxol-induced serine phosphorylation of the 66-kDa Shc isoform in A549 and RAW 264.7 cells. Biochim Biophys Acta 1590:76–83
42. Laviola L, Orlando MR, Incalza MA et al (2013) TNFα signals via p66(Shc) to induce E-selectin, promote leukocyte transmigration and enhance permeability in human endothelial cells. PLoS One 8:e81930
43. Pinton P, Rimessi A, Marchi S et al (2007) Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc. Science 315:659–663
44. Almeida M, Han L, Ambrogini E, Bartell SM, Manolagas SC (2010) Oxidative stress stimulates apoptosis and activates NF-κB in osteoblastic cells via a PKCβ/p66shc signaling cascade: counter regulation by estrogens or androgens. Mol Endocrinol 24:2030–2037
45. Sun L, Xiao L, Nie J et al (2010) p66Shc mediates high-glucose and angiotensin II-induced oxidative stress renal tubular injury via mitochondrial-dependent apoptotic pathway. Am J Physiol Ren Physiol 299:F1014–F1025
46. Oshikawa J, Kim SJ, Furuta E et al (2012) Novel role of p66Shc in ROS-dependent VEGF signaling and angiogenesis in endothelial cells. Am J Physiol Heart Circ Physiol 302:H724–H732
47. Giorgio M, Migliaccio E, Orsini F et al (2005) Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 122:221–233
48. Migliaccio E, Giorgio M, Pelicci PG (2006) Apoptosis and aging: role of p66Shc redox protein. Antioxid Redox Signal 8:600–608
49. Butler AE, Janson J, Bonner-Weir S, Ritzel R, Rizza RA, Butler PC (2003) Beta cell deficit and increased beta cell apoptosis in humans with type 2 diabetes. Diabetes 52:102–110
50. Zhou S, Chen HZ, Wan YZ et al (2011) Repression of p66Shc expression by SIRT1 contributes to the prevention of hyperglycemia-induced endothelial dysfunction. Circ Res 109:639–648